This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
7cys
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7cys is ON HOLD Authors: Yamane, M., Takenoya, M., Sue, M., Yajima, S. Description: Crystal structure of barley agmatine coumaroyltransferase (HvAC...) |
|||
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of barley agmatine coumaroyltransferase (HvACT), an N-acyltransferase in BAHD superfamily== | |
| + | <StructureSection load='7cys' size='340' side='right'caption='[[7cys]], [[Resolution|resolution]] 1.81Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7cys]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CYS FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7cys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cys OCA], [https://pdbe.org/7cys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cys RCSB], [https://www.ebi.ac.uk/pdbsum/7cys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cys ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/AGCT1_HORVU AGCT1_HORVU] Involved in the synthesis of hordatines (antifungal hydroxycinnamoylagmatine derivatives). Specific for agmatine as the acyl acceptor, inactive towards tyramine and putrescine. Has activity with the acyl donors 4-coumaroyl-CoA, cinnamoyl-CoA, caffeoyl-CoA, feruloyl-CoA, and to a lesser extent sinapoyl-CoA.<ref>PMID:12582168</ref> <ref>PMID:18270436</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The enzymes of the BAHD superfamily, a large group of acyl-CoA-dependent acyltransferases in plants, are involved in the biosynthesis of diverse secondary metabolites. While the structures of several O-acyltransferases from the BAHD superfamily, such as hydroxycinnamoyl-CoA shikimate hydroxycinnamoyl transferase, have been elucidated, no structural information on N-acyltransferases is available. Hordeum vulgare agmatine coumaroyltransferase (HvACT) is an N-acyltransferase from the BAHD superfamily and is one of the most important enzymes in the secondary metabolism of barley. Here, an apo-form structure of HvACT is reported as the first structure of an N-acyltransferase from the BAHD superfamily. HvACT crystals diffracted to 1.8 A resolution and belonged to the monoclinic space group P21, with unit-cell parameters a = 57.6, b = 59.5, c = 73.6 A, alpha = 90, beta = 91.3 , gamma = 90 degrees . Like other known BAHD superfamily structures, HvACT contains two domains that adopt a two-layer alphabeta-sandwich architecture and a solvent-exposed channel that penetrates the enzyme core. | ||
| - | + | Crystal structure of barley agmatine coumaroyltransferase, an N-acyltransferase from the BAHD superfamily.,Yamane M, Takenoya M, Yajima S, Sue M Acta Crystallogr F Struct Biol Commun. 2020 Dec 1;76(Pt 12):590-596. doi:, 10.1107/S2053230X20014880. Epub 2020 Nov 25. PMID:33263570<ref>PMID:33263570</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7cys" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Takenoya | + | <references/> |
| - | [[Category: Yajima | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Hordeum vulgare]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sue M]] | ||
| + | [[Category: Takenoya M]] | ||
| + | [[Category: Yajima S]] | ||
| + | [[Category: Yamane M]] | ||
Current revision
Crystal structure of barley agmatine coumaroyltransferase (HvACT), an N-acyltransferase in BAHD superfamily
| |||||||||||
